ArticleProceedings of the National Academy of Sciences of the United States of America2021
Structural and molecular basis of cross-seeding barriers in amyloids.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
What it found
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Who cites it
36 citing papers in PubMed, 63 citations in OpenAlex.
- Prion-like transmission and propagation of human β-amyloid to the bank vole rodent model.Acta neuropathologica · 2026Article
- Amelogenin proteolysis orchestrates functional amyloid pathways in enamel development.Matrix biology : journal of the International Society for Matrix Biology · 2026Article
- Regulated cell death in fungi from a comparative immunology perspective.Cell death and differentiation · 2026Review
- Structural basis for amyloid fibril assembly by the master cell-signaling regulator receptor-interacting protein kinase 1.Nature communications · 2025Article
- Article
- High-qualitySolid state nuclear magnetic resonance · 2025Article
- Structural basis ofScience advances · 2025Article
- Characterization of an amyloid-based antiphage defence system in Escherichia coli.Nature microbiology · 2025Article
- Harnessing deep learning for proteome-scale detection of amyloid signaling motifs.Bioinformatics (Oxford, England) · 2025Article
- Emerging biophysical origins and pathogenic implications of amyloid oligomers.Nature communications · 2025Review
- Guide to the structural characterization of protein aggregates and amyloid fibrils by CD spectroscopy.Protein science : a publication of the Protein Society · 2025Article
- The p3 peptides (AβNature communications · 2025Article
- Spiers Memorial Lecture: NMR crystallography.Faraday discussions · 2025Article
- Dipolar Recoupling in Rotating Solids.Chemical reviews · 2024Review
- Proteomic Evidence for Amyloidogenic Cross-Seeding in Fibrinaloid Microclots.International journal of molecular sciences · 2024Article
- Structure of biofilm-forming functional amyloid PSMα1 fromProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Atomic resolution structure of full-length human insulin fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Analytical Framework to Understand the Origins of Methyl Side-Chain Dynamics in Protein Assemblies.Journal of the American Chemical Society · 2024Article
- New views on the complex interplay between degeneration and autoimmunity in multiple sclerosis.Frontiers in cellular neuroscience · 2024Article
- Alzheimer's Progenitor Amyloid-β Targets and Dissolves Microbial Amyloids and Impairs Biofilm Function.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
Corrections and comments
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Authors and funding
15 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neurodegenerative disorders are frequently associated with β-sheet-rich amyloid deposits. Amyloid-forming proteins can aggregate under different structural conformations known as strains, which can exhibit a prion-like behavior and distinct pathophenotypes. Precise molecular determinants defining strain specificity and cross-strain interactions (cross-seeding) are currently unknown. The HET-s prion protein from the fungus
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.